J. Anim Sci.
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J. Anim Sci. 1984. 58:1437-1445.
© 1984 American Society of Animal Science

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Isolation-Perfusion of Ovine Hind Limbs. IV. Effects of Level of Activity on Amino Acid and Glucose Metabolism1,2,

W. W. Gill, L. C. Pendlum3, J. A. Boling, J. M. Koenig and T. O. Lindsey4

University of Kentucky, Lexington 40546

Abstract

Twenty-one wether lambs averaging 30.0 kg were utilized in a study to determine the influence of level of muscular activity (via electrical stimulation) on metabolism of amino acids and glucose of isolated-perfused hind limbs. Treatments consisted of: (1) control, (2) low electrical stimulation and (3) high electrical stimulation. Mean perfusion flow rate was unaffected by treatment or time of perfusion. Perfusion pressure and hematocrit were increased (P<.05) by stimulation. Glucose levels decreased from a pretreatment average of 44.7 to 41.3, 26.8 and 20.0 mg/dl for treatments 1 to 3, respectively. Lactic acid levels increased from the pretreatment mean of 37.7 to 46.7, 63.8 and 69.4 mg/dl, respectively. Plasma-free fatty acids were utilized from the perfusate at .84, .76 and .68 meq•liter–1·min–1, respectively. Perfusate urea N levels were unaffected by treatment or time of sampling, but perfusate ammonia levels increased in all treatments (ammonia levels for treatments 1 to 3 increased by .50, 1.09 and 1.47 mg/dl, respectively). Perfusate amino acid changes suggested a flux of some amino acids from muscle to perfusate due to electrical stimulation, but perfusate branched chain amino acid concentrations decreased in all treatment groups. Fifty microcuries of 14C-lysine were included in the initial perfusate. Total perfusate radioactivity in all treatments declined with time, reflective of lysine uptake by the muscle. Total perfusate lysine concentration changed less markedly, suggesting that muscle is contributing to maintenance of plasma amino acid levels. Muscle lysine uptake was highest for the control group and lowest at the high level of stimulation, indicating that cellular uptake and incorporation into muscle protein was impeded by muscular stimulation.


Footnotes

1 This paper (no. 82-5-25) is published with the approval of the Director of the Kentucky Agr. Exp. Sta.

2 Dept. of Anim. Sci.

3 Present address: Lilly Research Lab., Greenfield, IN 46140.

4 Present address: Smith Kline Animal Health, West Chester, PA 19380.







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Copyright © 1984 by the American Society of Animal Science.